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Related Concept Videos

Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibody Structure and Classes01:25

Antibody Structure and Classes

Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
Antibody Actions01:26

Antibody Actions

Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
Cross-reactivity00:42

Cross-reactivity

Overview

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Related Experiment Video

Updated: Jun 6, 2026

Chemical Conjugation of a Purified DEC-205-Directed Antibody with Full-Length Protein for Targeting Mouse Dendritic Cells In Vitro and In Vivo
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Chemical Conjugation of a Purified DEC-205-Directed Antibody with Full-Length Protein for Targeting Mouse Dendritic Cells In Vitro and In Vivo

Published on: February 5, 2021

Antibody dendrimers.

Hiroyasu Yamaguchi1, Akira Harada

  • 1Department of Macromolecular Science, Graduate School of Science, Osaka University, Osaka, 560-0043, Japan.

Topics in Current Chemistry
|December 7, 2010
PubMed
Summary
This summary is machine-generated.

Antibody supramolecular assemblies, including novel antibody dendrimers, enhance biosensor detection signals for antigens. This molecular recognition strategy offers amplified signal amplification for improved antigen detection.

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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

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Last Updated: Jun 6, 2026

Chemical Conjugation of a Purified DEC-205-Directed Antibody with Full-Length Protein for Targeting Mouse Dendritic Cells In Vitro and In Vivo
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Chemical Conjugation of a Purified DEC-205-Directed Antibody with Full-Length Protein for Targeting Mouse Dendritic Cells In Vitro and In Vivo

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Targeted Antibody Blocking by a Dual-Functional Conjugate of Antigenic Peptide and Fc-III Mimetics (DCAF)
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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

Area of Science:

  • Biochemistry
  • Materials Science
  • Immunology

Background:

  • Antibodies specifically recognize and bind to antigens, forming the basis of immune responses and diagnostic tools.
  • Supramolecular chemistry principles can be applied to engineer antibody assemblies for enhanced molecular recognition and signal transduction.

Purpose of the Study:

  • To investigate supramolecular formations of antibodies with antigens.
  • To develop novel antibody-based supramolecular architectures for enhanced biosensing applications.
  • To devise an amplification method for biosensor detection signals using antibody-antigen supramolecular assemblies.

Main Methods:

  • Construction of linear and network supramolecular architectures using immunoglobulin G (IgG) and multivalent antigens.
  • Design and preparation of dendritic supramolecular complexes (antibody dendrimers) using immunoglobulin M (IgM) or protein A/G as cores and IgGs as branches.
  • Utilizing surface plasmon resonance (SPR) biosensor technology to analyze signal amplification in antibody-antigen supramolecular assemblies.

Main Results:

  • Successfully constructed linear and network supramolecular architectures via antibody-antigen interactions.
  • Developed novel antibody dendrimers with a molecular weight of approximately 2 million, assembled via non-covalent bonds.
  • Demonstrated that antibody dendrimers bind antigens with high specificity and strong affinity.
  • Observed significant signal amplification for antigen detection using SPR biosensors with antibody dendrimers.

Conclusions:

  • Antibody supramolecular assemblies, particularly antibody dendrimers, offer a powerful strategy for enhancing antigen detection sensitivity in biosensors.
  • The developed antibody dendrimers exhibit excellent specificity and binding affinity for target antigens.
  • The supramolecular approach provides a novel amplification method for biosensing, leveraging enhanced molecular recognition and signal transduction.